Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous Abstract[Identification of Volatile Organic Compounds Used to Diagnose and Evaluate Acute Promyelocyte Leukemia]    Next AbstractDifferent senescent HDPE pipe-risk: brief field investigation from source water to tap water in China (Changsha City) »

Mol Cell Biol


Title:EH domain proteins Pan1p and End3p are components of a complex that plays a dual role in organization of the cortical actin cytoskeleton and endocytosis in Saccharomyces cerevisiae
Author(s):Tang HY; Munn A; Cai M;
Address:"Institute of Molecular and Cell Biology, National University of Singapore, Singapore"
Journal Title:Mol Cell Biol
Year:1997
Volume:17
Issue:8
Page Number:4294 - 4304
DOI: 10.1128/MCB.17.8.4294
ISSN/ISBN:0270-7306 (Print) 1098-5549 (Electronic) 0270-7306 (Linking)
Abstract:"Several proteins from diverse organisms have been shown to share a region of sequence homology with the mammalian epidermal growth factor receptor tyrosine kinase substrate Eps15. Included in this new protein family, termed EH domain proteins, are two yeast proteins, Pan1p and End3p. We have shown previously that Pan1p is required for normal organization of the actin cytoskeleton and that it associates with the actin patches on the cell cortex. End3p has been shown by others to be an important factor in the process of endocytosis. End3p is also known to be required for the organization of the actin cytoskeleton. Here we report that Pan1p and End3p act as a complex in vivo. Using the pan1-4 mutant which we isolated and characterized previously, the END3 gene was identified as a suppressor of pan1-4 when overexpressed. Suppression of the pan1-4 mutation by multicopy END3 required the presence of the mutant Pan1p protein. Coimmunoprecipitation and two-hybrid protein interaction experiments indicated that Pan1p and End3p associate with each other. The localization of Pan1p to the cortical actin cytoskeleton became weakened in the end3 mutant at the permissive temperature and undetectable at the restrictive temperature, suggesting that End3p may be important for proper localization of Pan1p to the cortical actin cytoskeleton. The finding that the pan1-4 mutant was defective in endocytosis as severely as the end3 mutant under nonpermissive conditions supports the notion that the association between Pan1p and End3p is of physiological relevance. Together with results of earlier reports, these results provide strong evidence suggesting that Pan1p and End3p are the components of a complex that has essential functions in both the organization of cell membrane-associated actin cytoskeleton and the process of endocytosis"
Keywords:"Actins/metabolism *Cytoskeletal Proteins Cytoskeleton/*metabolism Endocytosis/*genetics Fungal Proteins/genetics/*metabolism Genes, Fungal/genetics Genetic Complementation Test Mating Factor Peptides/metabolism Saccharomyces cerevisiae/*cytology/genetics/;"
Notes:"MedlineTang, H Y Munn, A Cai, M eng Research Support, Non-U.S. Gov't 1997/08/01 Mol Cell Biol. 1997 Aug; 17(8):4294-304. doi: 10.1128/MCB.17.8.4294"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 26-12-2024